Hackert, Philipp

[["dc.bibliographiccitation.artnumber","6152"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Krogh, Nicolai"],["dc.contributor.author","Pan, Kuan-Ting"],["dc.contributor.author","Jaafar, Mariam"],["dc.contributor.author","Henras, Anthony K."],["dc.contributor.author","Nielsen, Henrik"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-12-01T09:20:51Z"],["dc.date.available","2021-12-01T09:20:51Z"],["dc.date.issued","2021"],["dc.description.abstract","Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41467-021-26208-9"],["dc.identifier.pii","26208"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94285"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.title","The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Zhang, Ying"],["dc.contributor.author","De Laurentiis, Evelina"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Wahlig, Mascha"],["dc.contributor.author","Ranjan, Namit"],["dc.contributor.author","Gruseck, Simon"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Wölfle, Tina"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Rospert, Sabine"],["dc.date.accessioned","2021-04-14T08:28:39Z"],["dc.date.available","2021-04-14T08:28:39Z"],["dc.date.issued","2021"],["dc.description.abstract","The guided entry of tail-anchored proteins (GET) pathway assists in the posttranslational delivery of tail-anchored proteins, containing a single C-terminal transmembrane domain, to the ER. Here we uncover how the yeast GET pathway component Get4/5 facilitates capture of tail-anchored proteins by Sgt2, which interacts with tail-anchors and hands them over to the targeting component Get3. Get4/5 binds directly and with high affinity to ribosomes, positions Sgt2 close to the ribosomal tunnel exit, and facilitates the capture of tail-anchored proteins by Sgt2. The contact sites of Get4/5 on the ribosome overlap with those of SRP, the factor mediating cotranslational ER-targeting. Exposure of internal transmembrane domains at the tunnel exit induces high-affinity ribosome binding of SRP, which in turn prevents ribosome binding of Get4/5. In this way, the position of a transmembrane domain within nascent ER-targeted proteins mediates partitioning into either the GET or SRP pathway directly at the ribosomal tunnel exit."],["dc.identifier.doi","10.1038/s41467-021-20981-3"],["dc.identifier.pmid","33542241"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82670"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/220"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/139"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation","SFB 1190 | P16: Co-translationaler Einbau von Proteinen in die bakterielle Plasmamembran"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.relation.workinggroup","RG Rodnina"],["dc.rights","CC BY 4.0"],["dc.title","Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","209"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Kleiber, Nicole"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Stiller, Carina"],["dc.contributor.author","Heinrichs, Marleen"],["dc.contributor.author","Mai, Mandy Mong-Quyen"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2022-02-01T10:31:09Z"],["dc.date.available","2022-02-01T10:31:09Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Modified nucleotides in tRNAs are important determinants of folding, structure and function. Here we identify METTL8 as a mitochondrial matrix protein and active RNA methyltransferase responsible for installing m 3 C 32 in the human mitochondrial (mt-)tRNA Thr and mt-tRNA Ser(UCN) . METTL8 crosslinks to the anticodon stem loop (ASL) of many mt-tRNAs in cells, raising the question of how methylation target specificity is achieved. Dissection of mt-tRNA recognition elements revealed U 34 G 35 and t 6 A 37 /(ms 2 )i 6 A 37 , present concomitantly only in the ASLs of the two substrate mt-tRNAs, as key determinants for METTL8-mediated methylation of C 32 . Several lines of evidence demonstrate the influence of U 34 , G 35 , and the m 3 C 32 and t 6 A 37 /(ms 2 )i 6 A 37 modifications in mt-tRNA Thr/Ser(UCN) on the structure of these mt-tRNAs. Although mt-tRNA Thr/Ser(UCN) lacking METTL8-mediated m 3 C 32 are efficiently aminoacylated and associate with mitochondrial ribosomes, mitochondrial translation is mildly impaired by lack of METTL8. Together these results define the cellular targets of METTL8 and shed new light on the role of m 3 C 32 within mt-tRNAs."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.1038/s41467-021-27905-1"],["dc.identifier.pii","27905"],["dc.identifier.pmid","35017528"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98794"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/390"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/167"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The RNA methyltransferase METTL8 installs m3C32 in mitochondrial tRNAsThr/Ser(UCN) to optimise tRNA structure and mitochondrial translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","320"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Heininger, Annika U."],["dc.contributor.author","Hackert, Phillip"],["dc.contributor.author","Andreou, Alexandra Z."],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Memet, Indira"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2017-09-07T11:54:35Z"],["dc.date.available","2017-09-07T11:54:35Z"],["dc.date.issued","2016"],["dc.description.abstract","A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes."],["dc.description.sponsorship","Open-Access Publikationsfonds 2016"],["dc.identifier.doi","10.1080/15476286.2016.1142038"],["dc.identifier.gro","3141714"],["dc.identifier.isi","000372909600008"],["dc.identifier.pmid","26821976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/258"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5383"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Brüning, Lukas"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Davila Gallesio, Jimena"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2019-07-09T11:50:53Z"],["dc.date.available","2019-07-09T11:50:53Z"],["dc.date.issued","2018"],["dc.description.abstract","Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly."],["dc.identifier.doi","10.1038/s41467-018-07783-w"],["dc.identifier.pmid","30568249"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16022"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59850"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/48"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","54"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","68"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Choudhury, Priyanka"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Memet, Indira"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T18:15:16Z"],["dc.date.available","2020-12-10T18:15:16Z"],["dc.date.issued","2018"],["dc.description.abstract","Ribosome synthesis is an essential cellular process, and perturbation of human ribosome production is linked to cancer and genetic diseases termed ribosomopathies. During their assembly, pre-ribosomal particles undergo numerous structural rearrangements, which establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome biogenesis. RNA helicases are essential mediators of such remodelling events and here, we demonstrate that the DEAH-box RNA helicase DHX37 is required for maturation of the small ribosomal subunit in human cells. Our data reveal that the presence of DHX37 in early pre-ribosomal particles is monitored by a quality control pathway and that failure to recruit DHX37 leads to pre-rRNA degradation. Using an in vivo crosslinking approach, we show that DHX37 binds directly to the U3 small nucleolar RNA (snoRNA) and demonstrate that the catalytic activity of the helicase is required for dissociation of the U3 snoRNA from pre-ribosomal complexes. This is an important event during ribosome assembly as it enables formation of the central pseudoknot structure of the small ribosomal subunit. We identify UTP14A as a direct interaction partner of DHX37 and our data suggest that UTP14A can act as a cofactor that stimulates the activity of the helicase in the context of U3 snoRNA release."],["dc.identifier.doi","10.1080/15476286.2018.1556149"],["dc.identifier.pmid","30582406"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74797"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/56"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","The human RNA helicase DHX37 is required for release of the U3 snoRNP from pre-ribosomal particles"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4066"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","4084"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Krogh, Nicolai"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Gallesio, Jimena Davila"],["dc.contributor.author","van Nues, Robert W."],["dc.contributor.author","Schneider, Claudia"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Nielsen, Henrik"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-07-05T14:57:35Z"],["dc.date.available","2021-07-05T14:57:35Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract RNA helicases play important roles in diverse aspects of RNA metabolism through their functions in remodelling ribonucleoprotein complexes (RNPs), such as pre-ribosomes. Here, we show that the DEAD box helicase Dbp3 is required for efficient processing of the U18 and U24 intron-encoded snoRNAs and 2′-O-methylation of various sites within the 25S ribosomal RNA (rRNA) sequence. Furthermore, numerous box C/D snoRNPs accumulate on pre-ribosomes in the absence of Dbp3. Many snoRNAs guiding Dbp3-dependent rRNA modifications have overlapping pre-rRNA basepairing sites and therefore form mutually exclusive interactions with pre-ribosomes. Analysis of the distribution of these snoRNAs between pre-ribosome-associated and \\‘free\\’ pools demonstrated that many are almost exclusively associated with pre-ribosomal complexes. Our data suggest that retention of such snoRNPs on pre-ribosomes when Dbp3 is lacking may impede rRNA 2′-O-methylation by reducing the recycling efficiency of snoRNPs and by inhibiting snoRNP access to proximal target sites. The observation of substoichiometric rRNA modification at adjacent sites suggests that the snoRNPs guiding such modifications likely interact stochastically rather than hierarchically with their pre-rRNA target sites. Together, our data provide new insights into the dynamics of snoRNPs on pre-ribosomal complexes and the remodelling events occurring during the early stages of ribosome assembly."],["dc.description.abstract","Abstract RNA helicases play important roles in diverse aspects of RNA metabolism through their functions in remodelling ribonucleoprotein complexes (RNPs), such as pre-ribosomes. Here, we show that the DEAD box helicase Dbp3 is required for efficient processing of the U18 and U24 intron-encoded snoRNAs and 2′-O-methylation of various sites within the 25S ribosomal RNA (rRNA) sequence. Furthermore, numerous box C/D snoRNPs accumulate on pre-ribosomes in the absence of Dbp3. Many snoRNAs guiding Dbp3-dependent rRNA modifications have overlapping pre-rRNA basepairing sites and therefore form mutually exclusive interactions with pre-ribosomes. Analysis of the distribution of these snoRNAs between pre-ribosome-associated and ‘free’ pools demonstrated that many are almost exclusively associated with pre-ribosomal complexes. Our data suggest that retention of such snoRNPs on pre-ribosomes when Dbp3 is lacking may impede rRNA 2′-O-methylation by reducing the recycling efficiency of snoRNPs and by inhibiting snoRNP access to proximal target sites. The observation of substoichiometric rRNA modification at adjacent sites suggests that the snoRNPs guiding such modifications likely interact stochastically rather than hierarchically with their pre-rRNA target sites. Together, our data provide new insights into the dynamics of snoRNPs on pre-ribosomal complexes and the remodelling events occurring during the early stages of ribosome assembly."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1093/nar/gkab159"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87680"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-441"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.relation.orgunit","Institut für Molekularbiologie"],["dc.rights","CC BY-NC 4.0"],["dc.title","RNA helicase-mediated regulation of snoRNP dynamics on pre-ribosomes and rRNA 2′- O -methylation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7719"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","7733"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","van Tran, Nhan"],["dc.contributor.author","Ernst, Felix G M"],["dc.contributor.author","Hawley, Ben R"],["dc.contributor.author","Zorbas, Christiane"],["dc.contributor.author","Ulryck, Nathalie"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Bohnsack, Katherine E"],["dc.contributor.author","Bohnsack, Markus T"],["dc.contributor.author","Jaffrey, Samie R"],["dc.contributor.author","Graille, Marc"],["dc.contributor.author","Lafontaine, Denis L J"],["dc.date.accessioned","2020-12-10T18:19:36Z"],["dc.date.available","2020-12-10T18:19:36Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1093/nar/gkz619"],["dc.identifier.eissn","1362-4962"],["dc.identifier.issn","0305-1048"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16634"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75306"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]